Abstract
Cells are provided with well-defined receptor structures (signal receivers) which interact with their corresponding ligands (signal molecules) and initiate a signal transduction pathway resulting in a change of cellular behavior or metabolism (Stoddard et al. 1992). It is well established that cells from both eukaryotic protists (single-cell organisms) and from Metazoa (multicellular organisms) respond to signals emanating from the extracellular environment. The extracellular signals to which protists respond are mainly nutrients which diffuse to their surfaces, and in most cases cross the cell membrane. In addition, they are able to bind peptide hormones, e.g., insulin or adrenocorticotropic hormone, as in the unicellular Tetrahymena, by receptor-like structures (Köhidai et al. 1994). Based on experimental data obtained with Tetrahymena, it has been proposed that the survival of protists presupposes the operation of highly dynamic membrane structures capable of recognizing a variety of environmental signals, interactions which are stored in a form of “memory” and transmitted to the progeny generation (Csaba 1987, 1994). Hence, in unicellular eukaryotes, the membrane-bound receptor(s) have a nondetermined ability to recognize ligands and are initially not genetically programmed. In contrast, in Metazoa the receptors are genetically preprogrammed.
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References
Aroian RV, Koga M, Mendel JE, Ohshima Y, Sternberg PW (1993) The let-23 gene necessary for Caenorhabiditis elegans vulval inducation encodes a tyrosine kinase of the EGF receptor subfamily. Nature 348: 693–699
Barnes RD (1980) Invertebrate zoology, 4th edn. Saunders, Philadelphia
Beveren CV (1988) Overview of the tyrosine kinase oncogenes. In: Reddy EP, Skalka AM, Curran T (eds) The oncogene handbook. Elsevier, Amsterdam, pp 185–191
Borojevic R (1966) Etude experimentale de la différenciation des cellules de l’éponge au cours de son développement. Dev Biol 14: 130–153
Brenner S (1987) Phosphotransferase sequence homology. Nature 329: 21
Cooper JA, Esch FS, Taylor SS, Hunter T (1984) Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro. J Biol Chem 259: 7835–7841
Csaba G (1987) Why do hormone receptors arise? In: Csaba G (ed) Development of hormone receptors. Birkhäuser, Basel, pp 7–13
Csaba G (1994) Phylogeny and ontogeny of chemical signaling: origin and development of hormone receptors. Int Rev Cytol 155: 1–48
Cunningham BA, Hemperley JJ, Murray BA, Prediger EA, Brackenbury R and Edelman GM (1987) Neural cell adhesion molecule: structure, Ig-like domains, cell surface modulation and alternative RNA splicing. Science 236: 799–806
Dickerson RE, Geiss I (1969) The structure and action of proteins. Harper and Row, New York
Edelman GM, Crossin KL (1991) Cell adhesion molecules. Annu Rev Biochem 60: 155–190
Field KG, Olsen GJ, Lane DJ, Giovannoni SJ, Ghiselin MT, Raff EC, Pace NR, Raff RA (1988) Molecular phylogeny of the animal kingdom. Science 239: 748–753
Ganlulin V, Rinkevich B, Schäcke H, Kruse M, Müller IM, Müller WEG (1994) Cell adhesion receptors and nuclear receptors are highly conserved from the lowest metazoa (marine sponges) to vertebrates. Biol Chem Hoppe-Seyler 375: 583–588
Garrone R (1978) Phylogenesis of connective tissue. Karger, Basel
Geer P, Hunter T, Lindberg RA (1994) Receptor protein-tryosine kinases and their signal transduction pathways. Annu Rev Cell Biol 10: 251–337
Glenney JRJ (1992) Tyrosine-phosphorylated proteins: mediators of signal transduction from the tyrosine kinases. Biochim Biophys Acta 1134: 113–127
Hanks SK, Quinn AM (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol 200A: 38–62
Hanks SK, Quinn AM, Hunter T (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241: 42–52
Hao QL, Heisterkamp N, Groffen J (1989) Isolation and sequence analysis of a novel human tyrosine kinase gene. Mol Cell Biol 9: 1587–1593
Harrelson AL, Goodman CS (1988) Growth cone guidance in insects: fasciclin II is a member of the immunoglobulin superfamily. Science 242: 700–708
Henkart P, Humphreys S, Humphreys T (1973) Characterization of sponge aggregation factor. A unique proteoglycan complex. Biochemistry 12: 3045–3050
Hunter T (1991) Protein kinase classification. Methods Enzymol 200A: 3–37
Hunter T, Lindberg RA, Middlemas DS, Tracy S, Geer P vd (1992) Receptor protein kinases and phosphatases. Cold Spring Harbor Symp Quant Biol 58: 25–41
Knoll AH (1994) Proterozoic and early Cambrian protists: evidence for accelerating evolutionary tempo. Proc Natl Acad Sci USA 91: 6743–6750
Köhidai J, Karsa J, Csaba G (1994) Effects of hormones on Chemotaxis in Tetrahymena: investigations on receptor memory. Microbios 77: 75–85
Kolchanov NA, Lim HA (1994) Computer analysis of genetic macromolecules. World Scientific, Singapore
Kreuter MH, Robitzki A, Chang S, Steffen R, Michaelis M, Kljajic Z, Bachmann M, Schröder HC, Müller WEG (1992) Production of the cytostatic agent, aeroplysinin by the sponge Verongia aerophoba in in vitro culture. Comp Biochem Physiol 101C: 183–187
Kruse M, Mikoc A, Cetkovic H, Gamulin V, Rinkevich B, Müller IM, Müller WEG (1994) Molecular evidence for the presence of a developmental gene in the lowest animals: identification of a homeobox-like gene in the marine sponge Geodia cydonium Mech Ageing Dev 77: 43–54
Lee RH, Slate DI, Moretti R, AM KA, Crews P (1992) Marine sponge polyketide inhibitors of protein tyrosine kinase. Biochem Biophys Res Commun 184: 765–772
Livneh E, Glazer L, Segal D, Schlessinger J, Shilo BZ (1985) The Drosophila EGF receptor gene homolog: conservation of both hormone and kinase domains. Cell 40: 599–607
Marschalek R, Hofmann J, Schumann G, Bach M, Dingermann T (1993) Different organization of the tRNA-gene-associated repetitive element, DRE, in NC4-derived strains and in other wild-type Dictyostelium discoideum strains. Eur J Biochem 217: 627–631
Mehlhorn H (1989) Grudriß der Zoologie. Fisher, Stuttgart, pp 81–82
Morgan WR, Greenwald I (1993) Two novel transmembrane protein tyrosine kinases expressed during Caenorhabiditis elegans hypodermal development. Mol Cell Biol 13: 7133–7143
Moscona AA (1963) Studies on cell aggregation: demonstration of materials with selective cell-binding activity. Proc Natl Acad Sci USA 49: 742–747
Müller WEG (1982) Cell membranes in sponges. Int Rev Cytol 77: 129–181
Müller WEG (1995) Molecular phylogeny of Metazoa [animals]: monophyletic origin. Naturwissenschaften 82: 321–329
Müller WEG, Zahn RK (1973) Purification and characterization of a species- specific aggregation factor in sponges. Exp Cell Res 80: 95–104
Müller WEG, Zahn RK, Kurelec B, Müller I, Uhlenbruck G, Vaith P (1979) Aggregation of sponge cells; a novel mechanism of controlled intercellular adhesion, basing on the correlation between glycosyltransferases and glycosidases. J Biol Chem 254: 1280–1287
Müller WEG, Conrad J, Schröder C, Zahn RK, Kurelec B, Dreesbach K, Uhlenbruck G (1983) Characterization of the trimeric, self-recognizing Geodia cydonium lectin I. Eur J Biochem 133: 263–267
Müller WEG, Diehl-Seifert B, Gramzow M, Friese U, Renneisen K, Schröder HC (1988) Interrelation between extracellular adhesion proteins and extracellular matrix in reaggregation of dissociated sponge cells. Int Rev Cytol 111: 211–229
Müller WEG, Schröder HC, Müller IM, Gamulin V (1994a) Phylogenetic relationship of ubiquitin repeats of the polyubiquitin gene from the marine sponge Geodia cydonium. J Mol Evol 39: 369–377
Müller WEG, Schröder HC, Schäcke H, Müller IM, Gamulin V (1994b) Phylogenetic relationship of adhesion proteins and ubiquitin from the marine sponge Geodia cydonium. Endocytobiosis Cell Res 10: 185–204
Müller WEG, Müller IM, Rinkevich B, Gamulin V (1995) Molecular evolution: evidence for the monophyletic origin of multicellular animals. Naturwissenschaften 82: 36–38
Nishida Y, Hata M, Nishizuka Y, Rutter WJ, Ebina Y (1986) Cloning of a Drosophila cDNA encoding a polypeptide similar to the human insulin receptor precursor. Biochem Biophys Res Commun 141: 474–481
Ottilie S, Raulf F, Barnekow A, Hannig G, Schartl M (1992) Multiple src-related kinase genes, skr1–4, in the fresh water sponge Spongilla lacustris. Oncogene 7: 1625–1630
Pfeifer K, Frank W, Schröder HC, Gamulin V, Rinkevich B, Müller IM, Müller WEG (1993a) cDNA cloning of the polyubiquitin gene from the marine sponge Geodia cydonium which is preferentially expressed during reaggregation of cells. J Cell Sci 106: 545–554
Pfeifer K, Haasemann M, Ugarkovic D, Bretting H, Fahrenholz F, Müller WEG (1993b) S-type lectins occur also in invertebrates: unusual subunit composition and high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium. Glycobiol 3: 179–184
Russo WM, Lukas TJ, Cohen S, Staros VJ (1985) Identification of residues in the nucleotide binding site of the epidermal growth factor receptor-kinase. J Biol Chem 260: 5205–5208
Sadowski I, Stone JC, Pawson T (1985) A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Mol Cell Biol 6: 4396–4408
Sarma AS, Daum T, Müller WEG (1993) Secondary metabolites from marine sponges. Ullstein-Mosby, Berlin
Schäcke H, Schröder HC, Gamulin V, Rinkevich B, Müller IM, Müller WEG (1994a) Molecular cloning of a receptor tyrosine kinase from the marine sponge Geodia cydonium: a new member of the receptor tyrosine kinase class II family in invertebrates. Molec Membrane Biol 11: 101–107
Schäcke H, Müller WEG, Gamulin V, Rinkevich B (1994b) The Ig superfamily includes members from the lowest invertebrates to the highest vertebrates. Immunol Today 15: 497–498
Schäcke H, Rinkevich B, Gamulin V, Müller IM, Müller WEG (1994c): Immunoglobulin-like domain is present in the extracellular part of the receptor tyrosine kinase from the marine sponge Geodia cydonium. J Molec Recognition 7: 272–276
Schlessinger J, Ullrich A (1992) Growth factor signaling by tyrosine kinases. Neuron 9: 383–391
Seeger MA, Haffley L, Kaufman TC (1988) Characterization of amalgam: a member of the immunoglobulin superfamily from Drosophila. Cell 55: 589–600
Shishido E, Higashijima S, Emori Y, Saigo K (1993) Two EGF-receptor homologues of Drosophila: one is expressed in mesodermal primordium in early embryos. Development 117: 751–761
Shoelson SE, Chatterjee S, Chaudhuri M, White MF (1992) YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase. Proc Natl Acad Sci USA 89: 2027–2031
Stephens RM, Schneider TD (1992) Features of spliceosome evolution and function inferred from analysis of the information at human splice sites. J Mol Biol 228: 1124–1136
Stoddard BL, Biemann HP, Koshland DE (1992) Receptors and transmembrane signaling. Cold Spring Harbor Symp Quant Biol 54: 1–15
Sun H, Tonks NK (1994) The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem Sci 19: 480–485
Sun SC, Lindström I, Boman HG, Faye I, Schmidt O (1990) Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily. Science 250: 1729–1732
Ullrich A, Schlessinger J (1990) Signal transduction by receptors with tyrosine kinase activity. Cell 61: 203–212
Ullrich A, Bell JR, Chen EY, Herrera R, Tetruzzelli LM, Dull TJ, Gray A, Coussens L, Liao YC, Tsubokawa M, Mason A, Seeburg PH, Grunfeld C, Rosen OM, Ramachandran J (1985) Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 313: 756–761
Ullrich A, Gray A, Tarn AW, Yang-Feng T, Tsubokawa M, Collins C, Henzel W, LeBon T, Kathuria S, Chen E, Jacobs S, Francke U, Ramachandran J, Fujita-Yamagushi Y (1986) Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J 5: 2503–2512
Van Hejine G (1987) Sequence analysis in molecular biology. Treasure Trove of Trivial Pursuit. Academic Press, London
Williams AF, Barclay AN (1988) The immunoglobulin superfamily — domains for cell surface recognition. Annu Rev Immunol 6: 381–405
Zarkower D, Stephenson P, Sheets M, Wickens M (1986) The AAUAAA sequence is required both for cleavage and for polyadenylation of Simian Virus 40 pre-mRNA in vitro. Mol Cell Biol 6: 2317–2323
Wilson HV (1907) On some phenomena of coalescence and regeneration in sponges. J Exp Zool 5: 245–258
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Müller, W.E.G., Schäcke, H. (1996). Characterization of the Receptor Protein-Tyrosine Kinase Gene from the Marine Sponge Geodia cydonium . In: Csaba, G., Müller, W.E.G. (eds) Signaling Mechanisms in Protozoa and Invertebrates. Progress in Molecular and Subcellular Biology, vol 17. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80106-8_9
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DOI: https://doi.org/10.1007/978-3-642-80106-8_9
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